Literature DB >> 21700217

No country for old misfolded glycoproteins.

Vladimir Denic1.   

Abstract

Gauss et al. (2011) present evidence that an endoplasmic reticulum (ER) sugar-removing enzyme with a folding sensor subunit enables a stochastic quality control mechanism, which marks with increasing probability misfolded glycoproteins for destruction the longer they reside in the ER.
Copyright © 2011 Elsevier Inc. All rights reserved.

Entities:  

Year:  2011        PMID: 21700217      PMCID: PMC3632639          DOI: 10.1016/j.molcel.2011.06.004

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


  11 in total

Review 1.  Posttranslational quality control: folding, refolding, and degrading proteins.

Authors:  S Wickner; M R Maurizi; S Gottesman
Journal:  Science       Date:  1999-12-03       Impact factor: 47.728

Review 2.  Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.

Authors:  Alexander Buchberger; Bernd Bukau; Thomas Sommer
Journal:  Mol Cell       Date:  2010-10-22       Impact factor: 17.970

3.  A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation.

Authors:  Vladimir Denic; Erin M Quan; Jonathan S Weissman
Journal:  Cell       Date:  2006-07-28       Impact factor: 41.582

4.  A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery.

Authors:  Robert Gauss; Ernst Jarosch; Thomas Sommer; Christian Hirsch
Journal:  Nat Cell Biol       Date:  2006-07-16       Impact factor: 28.824

5.  The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.

Authors:  Geng Tian; Song Xiang; Robert Noiva; William J Lennarz; Hermann Schindelin
Journal:  Cell       Date:  2006-01-13       Impact factor: 41.582

6.  A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum.

Authors:  Robert Gauss; Kazue Kanehara; Pedro Carvalho; Davis T W Ng; Markus Aebi
Journal:  Mol Cell       Date:  2011-06-24       Impact factor: 17.970

7.  Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation.

Authors:  Machiko Sakoh-Nakatogawa; Shuh-Ichi Nishikawa; Toshiya Endo
Journal:  J Biol Chem       Date:  2009-03-11       Impact factor: 5.157

8.  Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system.

Authors:  Wei Xie; Kazue Kanehara; Ayaz Sayeed; Davis T W Ng
Journal:  Mol Biol Cell       Date:  2009-05-20       Impact factor: 4.138

9.  Defining the glycan destruction signal for endoplasmic reticulum-associated degradation.

Authors:  Erin M Quan; Yukiko Kamiya; Daiki Kamiya; Vladimir Denic; Jimena Weibezahn; Koichi Kato; Jonathan S Weissman
Journal:  Mol Cell       Date:  2008-12-26       Impact factor: 17.970

10.  Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum.

Authors:  Simone Clerc; Christian Hirsch; Daniela Maria Oggier; Paola Deprez; Claude Jakob; Thomas Sommer; Markus Aebi
Journal:  J Cell Biol       Date:  2009-01-05       Impact factor: 10.539

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  1 in total

1.  Htm1p-Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation.

Authors:  Yi-Chang Liu; Danica Galonić Fujimori; Jonathan S Weissman
Journal:  Proc Natl Acad Sci U S A       Date:  2016-06-28       Impact factor: 11.205

  1 in total

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